GenomeNet

Database: PDB
Entry: 3K7T
LinkDB: 3K7T
Original site: 3K7T 
HEADER    OXIDOREDUCTASE                          13-OCT-09   3K7T              
TITLE     CRYSTAL STRUCTURE OF APO-FORM 6-HYDROXY-L-NICOTINE OXIDASE, CRYSTAL   
TITLE    2 FORM P3121                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6-HYDROXY-L-NICOTINE OXIDASE;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.5.3.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARTHROBACTER NICOTINOVORANS;                    
SOURCE   3 ORGANISM_TAXID: 29320;                                               
SOURCE   4 GENE: 6-HLNO;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM105;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    ENANTIOMERIC SUBSTRATES, FLAVOENZYMES, NICOTINE DEGRADATION, OXIDASE, 
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.P.BOURENKOV,G.S.KACHALOVA,H.D.BARTUNIK                              
REVDAT   4   06-SEP-23 3K7T    1       REMARK                                   
REVDAT   3   01-NOV-17 3K7T    1       REMARK                                   
REVDAT   2   02-MAR-10 3K7T    1       JRNL                                     
REVDAT   1   19-JAN-10 3K7T    0                                                
JRNL        AUTH   G.S.KACHALOVA,G.P.BOURENKOV,T.MENGESDORF,S.SCHENK,H.R.MAUN,  
JRNL        AUTH 2 M.BURGHAMMER,C.RIEKEL,K.DECKER,H.D.BARTUNIK                  
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF FREE AND SUBSTRATE-BOUND       
JRNL        TITL 2 6-HYDROXY-L-NICOTINE OXIDASE FROM ARTHROBACTER               
JRNL        TITL 3 NICOTINOVORANS.                                              
JRNL        REF    J.MOL.BIOL.                   V. 396   785 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20006620                                                     
JRNL        DOI    10.1016/J.JMB.2009.12.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 38462                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.278                           
REMARK   3   R VALUE            (WORKING SET) : 0.275                           
REMARK   3   FREE R VALUE                     : 0.321                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2035                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2792                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 134                          
REMARK   3   BIN FREE R VALUE                    : 0.4570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6540                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 192                                     
REMARK   3   SOLVENT ATOMS            : 42                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.72000                                              
REMARK   3    B22 (A**2) : 3.72000                                              
REMARK   3    B33 (A**2) : -5.58000                                             
REMARK   3    B12 (A**2) : 1.86000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.621         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.393         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.345         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.930        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6890 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9374 ; 1.781 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   848 ; 7.599 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   306 ;36.675 ;23.595       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1054 ;18.815 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;17.515 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1030 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5236 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3139 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4594 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   237 ; 0.167 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    34 ; 0.294 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4286 ; 1.021 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6750 ; 1.853 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2979 ; 2.467 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2624 ; 4.256 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3K7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055654.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.75000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLREP                       
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3K7M                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.5M LITHIUM SULFATE, PH     
REMARK 280  7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.63933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      133.27867            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      133.27867            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       66.63933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 425    CB   OG                                             
REMARK 470     SER B 425    CB   OG                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 370   C   -  N   -  CD  ANGL. DEV. = -12.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  92       45.05    -97.53                                   
REMARK 500    LYS A 129     -147.53    -84.99                                   
REMARK 500    HIS A 187       56.49    -94.31                                   
REMARK 500    TYR A 189       70.10     40.72                                   
REMARK 500    SER A 232      -81.34    -54.91                                   
REMARK 500    LYS A 241      -82.67    -12.95                                   
REMARK 500    ASP A 242       71.35    -67.09                                   
REMARK 500    HIS A 244      179.24    -53.40                                   
REMARK 500    ALA A 254       41.62   -108.79                                   
REMARK 500    TYR A 313      -71.36   -105.89                                   
REMARK 500    SER A 317     -157.50   -151.45                                   
REMARK 500    PHE A 367      -50.53   -133.75                                   
REMARK 500    PRO A 370      -76.04    -95.13                                   
REMARK 500    HIS A 383      -55.24   -155.43                                   
REMARK 500    ASP B 135       63.95     60.60                                   
REMARK 500    ASP B 151       85.21     57.11                                   
REMARK 500    HIS B 187       42.01    -87.83                                   
REMARK 500    LEU B 196       42.82    -80.72                                   
REMARK 500    LEU B 198       81.30    -68.52                                   
REMARK 500    ASP B 199      -81.86   -106.58                                   
REMARK 500    TYR B 313      -70.77   -100.47                                   
REMARK 500    THR B 327     -157.63   -158.87                                   
REMARK 500    PHE B 367      -51.13   -130.77                                   
REMARK 500    PRO B 370      -88.76   -108.32                                   
REMARK 500    HIS B 383      -72.06   -140.39                                   
REMARK 500    ALA B 390       54.36   -102.98                                   
REMARK 500    PHE B 404       79.41   -151.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GP7 A  435                                                       
REMARK 610     GP7 B  435                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP7 A 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP7 B 435                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K7M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF 6-HYDROXY-L-NICOTINE OXIDASE FROM ARTHROBACTER  
REMARK 900 NICOTINOVORANS                                                       
REMARK 900 RELATED ID: 3K7Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SUBSTRATE-BOUND 6-HYDROXY-L-NICOTINE OXIDASE    
REMARK 900 FROM ARTHROBACTER NICOTINOVORANS                                     
DBREF  3K7T A    1   425  UNP    Q93NH4   Q93NH4_ARTNI     1    425             
DBREF  3K7T B    1   425  UNP    Q93NH4   Q93NH4_ARTNI     1    425             
SEQRES   1 A  425  MET TYR ASP ALA ILE VAL VAL GLY GLY GLY PHE SER GLY          
SEQRES   2 A  425  LEU LYS ALA ALA ARG ASP LEU THR ASN ALA GLY LYS LYS          
SEQRES   3 A  425  VAL LEU LEU LEU GLU GLY GLY GLU ARG LEU GLY GLY ARG          
SEQRES   4 A  425  ALA TYR SER ARG GLU SER ARG ASN VAL PRO GLY LEU ARG          
SEQRES   5 A  425  VAL GLU ILE GLY GLY ALA TYR LEU HIS ARG LYS HIS HIS          
SEQRES   6 A  425  PRO ARG LEU ALA ALA GLU LEU ASP ARG TYR GLY ILE PRO          
SEQRES   7 A  425  THR ALA ALA ALA SER GLU PHE THR SER PHE ARG HIS ARG          
SEQRES   8 A  425  LEU GLY PRO THR ALA VAL ASP GLN ALA PHE PRO ILE PRO          
SEQRES   9 A  425  GLY SER GLU ALA VAL ALA VAL GLU ALA ALA THR TYR THR          
SEQRES  10 A  425  LEU LEU ARG ASP ALA HIS ARG ILE ASP LEU GLU LYS GLY          
SEQRES  11 A  425  LEU GLU ASN GLN ASP LEU GLU ASP LEU ASP ILE PRO LEU          
SEQRES  12 A  425  ASN GLU TYR VAL ASP LYS LEU ASP LEU PRO PRO VAL SER          
SEQRES  13 A  425  ARG GLN PHE LEU LEU ALA TRP ALA TRP ASN MET LEU GLY          
SEQRES  14 A  425  GLN PRO ALA ASP GLN ALA SER ALA LEU TRP MET LEU GLN          
SEQRES  15 A  425  LEU VAL ALA ALA HIS HIS TYR SER ILE LEU GLY VAL VAL          
SEQRES  16 A  425  LEU SER LEU ASP GLU VAL PHE SER ASN GLY SER ALA ASP          
SEQRES  17 A  425  LEU VAL ASP ALA MET SER GLN GLU ILE PRO GLU ILE ARG          
SEQRES  18 A  425  LEU GLN THR VAL VAL THR GLY ILE ASP GLN SER GLY ASP          
SEQRES  19 A  425  VAL VAL ASN VAL THR VAL LYS ASP GLY HIS ALA PHE GLN          
SEQRES  20 A  425  ALA HIS SER VAL ILE VAL ALA THR PRO MET ASN THR TRP          
SEQRES  21 A  425  ARG ARG ILE VAL PHE THR PRO ALA LEU PRO GLU ARG ARG          
SEQRES  22 A  425  ARG SER VAL ILE GLU GLU GLY HIS GLY GLY GLN GLY LEU          
SEQRES  23 A  425  LYS ILE LEU ILE HIS VAL ARG GLY ALA GLU ALA GLY ILE          
SEQRES  24 A  425  GLU CYS VAL GLY ASP GLY ILE PHE PRO THR LEU TYR ASP          
SEQRES  25 A  425  TYR CYS GLU VAL SER GLU SER GLU ARG LEU LEU VAL ALA          
SEQRES  26 A  425  PHE THR ASP SER GLY SER PHE ASP PRO THR ASP ILE GLY          
SEQRES  27 A  425  ALA VAL LYS ASP ALA VAL LEU TYR TYR LEU PRO GLU VAL          
SEQRES  28 A  425  GLU VAL LEU GLY ILE ASP TYR HIS ASP TRP ILE ALA ASP          
SEQRES  29 A  425  PRO LEU PHE GLU GLY PRO TRP VAL ALA PRO ARG VAL GLY          
SEQRES  30 A  425  GLN PHE SER ARG VAL HIS LYS GLU LEU GLY GLU PRO ALA          
SEQRES  31 A  425  GLY ARG ILE HIS PHE VAL GLY SER ASP VAL SER LEU GLU          
SEQRES  32 A  425  PHE PRO GLY TYR ILE GLU GLY ALA LEU GLU THR ALA GLU          
SEQRES  33 A  425  CYS ALA VAL ASN ALA ILE LEU HIS SER                          
SEQRES   1 B  425  MET TYR ASP ALA ILE VAL VAL GLY GLY GLY PHE SER GLY          
SEQRES   2 B  425  LEU LYS ALA ALA ARG ASP LEU THR ASN ALA GLY LYS LYS          
SEQRES   3 B  425  VAL LEU LEU LEU GLU GLY GLY GLU ARG LEU GLY GLY ARG          
SEQRES   4 B  425  ALA TYR SER ARG GLU SER ARG ASN VAL PRO GLY LEU ARG          
SEQRES   5 B  425  VAL GLU ILE GLY GLY ALA TYR LEU HIS ARG LYS HIS HIS          
SEQRES   6 B  425  PRO ARG LEU ALA ALA GLU LEU ASP ARG TYR GLY ILE PRO          
SEQRES   7 B  425  THR ALA ALA ALA SER GLU PHE THR SER PHE ARG HIS ARG          
SEQRES   8 B  425  LEU GLY PRO THR ALA VAL ASP GLN ALA PHE PRO ILE PRO          
SEQRES   9 B  425  GLY SER GLU ALA VAL ALA VAL GLU ALA ALA THR TYR THR          
SEQRES  10 B  425  LEU LEU ARG ASP ALA HIS ARG ILE ASP LEU GLU LYS GLY          
SEQRES  11 B  425  LEU GLU ASN GLN ASP LEU GLU ASP LEU ASP ILE PRO LEU          
SEQRES  12 B  425  ASN GLU TYR VAL ASP LYS LEU ASP LEU PRO PRO VAL SER          
SEQRES  13 B  425  ARG GLN PHE LEU LEU ALA TRP ALA TRP ASN MET LEU GLY          
SEQRES  14 B  425  GLN PRO ALA ASP GLN ALA SER ALA LEU TRP MET LEU GLN          
SEQRES  15 B  425  LEU VAL ALA ALA HIS HIS TYR SER ILE LEU GLY VAL VAL          
SEQRES  16 B  425  LEU SER LEU ASP GLU VAL PHE SER ASN GLY SER ALA ASP          
SEQRES  17 B  425  LEU VAL ASP ALA MET SER GLN GLU ILE PRO GLU ILE ARG          
SEQRES  18 B  425  LEU GLN THR VAL VAL THR GLY ILE ASP GLN SER GLY ASP          
SEQRES  19 B  425  VAL VAL ASN VAL THR VAL LYS ASP GLY HIS ALA PHE GLN          
SEQRES  20 B  425  ALA HIS SER VAL ILE VAL ALA THR PRO MET ASN THR TRP          
SEQRES  21 B  425  ARG ARG ILE VAL PHE THR PRO ALA LEU PRO GLU ARG ARG          
SEQRES  22 B  425  ARG SER VAL ILE GLU GLU GLY HIS GLY GLY GLN GLY LEU          
SEQRES  23 B  425  LYS ILE LEU ILE HIS VAL ARG GLY ALA GLU ALA GLY ILE          
SEQRES  24 B  425  GLU CYS VAL GLY ASP GLY ILE PHE PRO THR LEU TYR ASP          
SEQRES  25 B  425  TYR CYS GLU VAL SER GLU SER GLU ARG LEU LEU VAL ALA          
SEQRES  26 B  425  PHE THR ASP SER GLY SER PHE ASP PRO THR ASP ILE GLY          
SEQRES  27 B  425  ALA VAL LYS ASP ALA VAL LEU TYR TYR LEU PRO GLU VAL          
SEQRES  28 B  425  GLU VAL LEU GLY ILE ASP TYR HIS ASP TRP ILE ALA ASP          
SEQRES  29 B  425  PRO LEU PHE GLU GLY PRO TRP VAL ALA PRO ARG VAL GLY          
SEQRES  30 B  425  GLN PHE SER ARG VAL HIS LYS GLU LEU GLY GLU PRO ALA          
SEQRES  31 B  425  GLY ARG ILE HIS PHE VAL GLY SER ASP VAL SER LEU GLU          
SEQRES  32 B  425  PHE PRO GLY TYR ILE GLU GLY ALA LEU GLU THR ALA GLU          
SEQRES  33 B  425  CYS ALA VAL ASN ALA ILE LEU HIS SER                          
HET    FAD  A 434      53                                                       
HET    GP7  A 435      43                                                       
HET    FAD  B 434      53                                                       
HET    GP7  B 435      43                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GP7 (1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-          
HETNAM   2 GP7  [(PENTADECANOYLOXY)METHYL]ETHYL (12E)-HEXADECA-9,12-            
HETNAM   3 GP7  DIENOATE                                                        
HETSYN     GP7 1-PENTADECANOYL-2-HEXADECANOYL-SN-GLYCERO-3-                     
HETSYN   2 GP7  PHOSPHOETHANOLAMINE                                             
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  GP7    2(C36 H68 N O8 P)                                            
FORMUL   7  HOH   *42(H2 O)                                                     
HELIX    1   1 GLY A   10  GLY A   24  1                                  15    
HELIX    2   2 HIS A   65  GLY A   76  1                                  12    
HELIX    3   3 GLU A  107  ARG A  124  1                                  18    
HELIX    4   4 LEU A  136  ASP A  140  5                                   5    
HELIX    5   5 PRO A  142  ASP A  151  1                                  10    
HELIX    6   6 PRO A  153  LEU A  168  1                                  16    
HELIX    7   7 SER A  176  HIS A  187  1                                  12    
HELIX    8   8 SER A  206  GLN A  215  1                                  10    
HELIX    9   9 PRO A  256  ILE A  263  5                                   8    
HELIX   10  10 PRO A  270  GLY A  280  1                                  11    
HELIX   11  11 ASP A  336  TYR A  346  1                                  11    
HELIX   12  12 GLY A  377  VAL A  382  1                                   6    
HELIX   13  13 LYS A  384  GLU A  388  5                                   5    
HELIX   14  14 TYR A  407  HIS A  424  1                                  18    
HELIX   15  15 GLY B   10  GLY B   24  1                                  15    
HELIX   16  16 HIS B   65  ASP B   73  1                                   9    
HELIX   17  17 PRO B  104  SER B  106  5                                   3    
HELIX   18  18 GLU B  107  ARG B  124  1                                  18    
HELIX   19  19 PRO B  142  ASP B  151  1                                  10    
HELIX   20  20 PRO B  153  GLY B  169  1                                  17    
HELIX   21  21 SER B  176  HIS B  187  1                                  12    
HELIX   22  22 ILE B  191  LEU B  196  1                                   6    
HELIX   23  23 SER B  206  GLN B  215  1                                  10    
HELIX   24  24 PRO B  256  TRP B  260  5                                   5    
HELIX   25  25 PRO B  270  GLU B  278  1                                   9    
HELIX   26  26 ASP B  336  TYR B  346  1                                  11    
HELIX   27  27 GLY B  377  VAL B  382  1                                   6    
HELIX   28  28 HIS B  383  GLU B  388  5                                   6    
HELIX   29  29 TYR B  407  HIS B  424  1                                  18    
SHEET    1   A 7 ILE A 220  ARG A 221  0                                        
SHEET    2   A 7 VAL A  27  LEU A  30  1  N  LEU A  29   O  ARG A 221           
SHEET    3   A 7 TYR A   2  VAL A   7  1  N  VAL A   6   O  LEU A  28           
SHEET    4   A 7 ALA A 245  VAL A 253  1  O  ILE A 252   N  VAL A   7           
SHEET    5   A 7 VAL A 236  VAL A 240 -1  N  VAL A 238   O  PHE A 246           
SHEET    6   A 7 VAL A 226  ASP A 230 -1  N  ASP A 230   O  ASN A 237           
SHEET    7   A 7 VAL A 264  THR A 266  1  O  VAL A 264   N  THR A 227           
SHEET    1   B 5 ILE A 220  ARG A 221  0                                        
SHEET    2   B 5 VAL A  27  LEU A  30  1  N  LEU A  29   O  ARG A 221           
SHEET    3   B 5 TYR A   2  VAL A   7  1  N  VAL A   6   O  LEU A  28           
SHEET    4   B 5 ALA A 245  VAL A 253  1  O  ILE A 252   N  VAL A   7           
SHEET    5   B 5 ILE A 393  PHE A 395  1  O  HIS A 394   N  VAL A 251           
SHEET    1   C 2 SER A  42  GLU A  44  0                                        
SHEET    2   C 2 ARG A  52  GLU A  54 -1  O  VAL A  53   N  ARG A  43           
SHEET    1   D 2 THR A  79  ALA A  81  0                                        
SHEET    2   D 2 GLU A 200  PHE A 202 -1  O  VAL A 201   N  ALA A  80           
SHEET    1   E 6 SER A  87  PHE A  88  0                                        
SHEET    2   E 6 ILE A 299  VAL A 302  1  O  GLU A 300   N  SER A  87           
SHEET    3   E 6 THR A 309  GLU A 315 -1  O  LEU A 310   N  CYS A 301           
SHEET    4   E 6 GLU A 320  ASP A 328 -1  O  LEU A 322   N  TYR A 313           
SHEET    5   E 6 GLY A 285  ARG A 293 -1  N  LEU A 286   O  THR A 327           
SHEET    6   E 6 GLU A 352  TYR A 358 -1  O  LEU A 354   N  HIS A 291           
SHEET    1   F 7 GLU B 219  ARG B 221  0                                        
SHEET    2   F 7 VAL B  27  LEU B  30  1  N  LEU B  29   O  GLU B 219           
SHEET    3   F 7 TYR B   2  VAL B   7  1  N  VAL B   6   O  LEU B  28           
SHEET    4   F 7 PHE B 246  VAL B 253  1  O  ILE B 252   N  VAL B   7           
SHEET    5   F 7 VAL B 236  VAL B 240 -1  N  VAL B 238   O  PHE B 246           
SHEET    6   F 7 VAL B 226  ASP B 230 -1  N  ASP B 230   O  ASN B 237           
SHEET    7   F 7 VAL B 264  THR B 266  1  O  VAL B 264   N  ILE B 229           
SHEET    1   G 5 GLU B 219  ARG B 221  0                                        
SHEET    2   G 5 VAL B  27  LEU B  30  1  N  LEU B  29   O  GLU B 219           
SHEET    3   G 5 TYR B   2  VAL B   7  1  N  VAL B   6   O  LEU B  28           
SHEET    4   G 5 PHE B 246  VAL B 253  1  O  ILE B 252   N  VAL B   7           
SHEET    5   G 5 ILE B 393  PHE B 395  1  O  HIS B 394   N  VAL B 251           
SHEET    1   H 2 SER B  42  GLU B  44  0                                        
SHEET    2   H 2 ARG B  52  GLU B  54 -1  O  VAL B  53   N  ARG B  43           
SHEET    1   I 2 THR B  79  ALA B  81  0                                        
SHEET    2   I 2 GLU B 200  PHE B 202 -1  O  VAL B 201   N  ALA B  80           
SHEET    1   J 6 SER B  87  PHE B  88  0                                        
SHEET    2   J 6 ILE B 299  VAL B 302  1  O  GLU B 300   N  SER B  87           
SHEET    3   J 6 THR B 309  GLU B 315 -1  O  ASP B 312   N  ILE B 299           
SHEET    4   J 6 GLU B 320  ASP B 328 -1  O  VAL B 324   N  TYR B 311           
SHEET    5   J 6 GLY B 285  ARG B 293 -1  N  VAL B 292   O  ARG B 321           
SHEET    6   J 6 GLU B 352  TYR B 358 -1  O  LEU B 354   N  HIS B 291           
CISPEP   1 THR A  266    PRO A  267          0        -3.01                     
CISPEP   2 HIS B  244    ALA B  245          0         2.20                     
CISPEP   3 THR B  266    PRO B  267          0        -2.06                     
SITE     1 AC1 28 GLY A   8  GLY A  10  PHE A  11  SER A  12                    
SITE     2 AC1 28 LEU A  30  GLU A  31  GLY A  32  GLY A  37                    
SITE     3 AC1 28 GLY A  38  ARG A  39  ALA A  40  GLY A  56                    
SITE     4 AC1 28 GLY A  57  TYR A  59  THR A 224  VAL A 226                    
SITE     5 AC1 28 ALA A 254  THR A 255  PRO A 256  LEU A 366                    
SITE     6 AC1 28 PHE A 367  TRP A 371  GLY A 397  SER A 398                    
SITE     7 AC1 28 GLY A 406  TYR A 407  ILE A 408  ALA A 411                    
SITE     1 AC2 12 GLN A  99  ALA A 100  THR A 115  PHE A 159                    
SITE     2 AC2 12 LEU A 160  MET A 180  ILE A 191  LEU A 192                    
SITE     3 AC2 12 VAL A 195  ILE B 103  GLY B 105  ALA B 108                    
SITE     1 AC3 32 VAL B   7  GLY B   8  GLY B  10  PHE B  11                    
SITE     2 AC3 32 SER B  12  LEU B  30  GLU B  31  GLY B  32                    
SITE     3 AC3 32 GLY B  37  GLY B  38  ARG B  39  GLY B  56                    
SITE     4 AC3 32 GLY B  57  TYR B  59  THR B 224  VAL B 225                    
SITE     5 AC3 32 VAL B 226  ALA B 254  THR B 255  PRO B 256                    
SITE     6 AC3 32 ILE B 263  TRP B 361  LEU B 366  PHE B 367                    
SITE     7 AC3 32 PRO B 370  GLY B 397  SER B 398  GLY B 406                    
SITE     8 AC3 32 TYR B 407  ILE B 408  ALA B 411  HOH B 519                    
SITE     1 AC4 12 ILE A 103  PRO A 104  GLY A 105  ALA B 100                    
SITE     2 AC4 12 VAL B 111  THR B 115  PHE B 159  LEU B 160                    
SITE     3 AC4 12 MET B 180  ILE B 191  LEU B 192  VAL B 195                    
CRYST1  122.957  122.957  199.918  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008133  0.004696  0.000000        0.00000                         
SCALE2      0.000000  0.009391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005002        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system